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Laminin-1 Phosphorylation by Protein Kinase A : Effect on self assembly and heparin binding
Koliakos, George,Koliakos, Kokkona Kouzi,Triantos, Athanasios,Trachana, Varvara,Kavoukopoulos, Evaggelos,Gaitatzi, Mary,Dimitriadou, Aphrodite 생화학분자생물학회 2001 BMB Reports Vol.33 No.5
Incubation of purified lamininl-nidogenl complexes with [γ-^(32)P]-ATP in the presence of the catalytic subunit of the protein kinase A (CAMP-dependent protein kinase) resulted in the phosphoryla6on of the alpha chain of laminin-1 and of the nidogen-1 molecule. Aminoacid electrophoresis indicated that phosphate was incorporated on serine residues. The phosphorylation effect of laminin-1 on the process of self assembly was studied by turbidometry In these experiments, the phosphorylated laminin-1 showed a reduced maximal aggregatjon capacity in comparison to the non-phosphorylated molecule. Examination of the laminin1 network under the electron microscope showed that the phosphorylated sample formed mainly linear extended oligomers, in contrast to controls that formed large and dense multimeric aggregates. Heparin binding on phosphorylated laminin-1 in comparison to controls was also tested using solid-phase binding assays. The results indicated an enhanced heparin binding to the phosphorylated protein. The results of this study indicate that lamininl-nidogenl is a substrate for protein kinase A in vitro. This phosphorylation had an obvious influence on the lamininl-nidogenl network formation and the heparin binding capacity of this molecule. However, further studies are needed to investigate whether or not this phenomenon could play a role in the formation of the structure of basement membranes in vivo.
Laminin-1 Phosphorylation by Protein Kinase A: Effect on self assembly and heparin binding
Koliakos, George,Kouzi-Koliakos, Kokkona,Triantos, Athanasios,Trachana, Varvara,Kavoukopoulos, Evaggelos,Gaitatzi, Mary,Dimitriadou, Aphrodite Korean Society for Biochemistry and Molecular Biol 2000 Journal of biochemistry and molecular biology Vol.33 No.5
Incubation of purified laminin1-nidogen1 complexes with $[{\gamma}-^{32}P]-ATP$ in the presence of the catalytic subunit of the protein kinase A (cAMP-dependent protein kinase) resulted in the phosphorylation of the alpha chain of laminin-1 and of the nidogen-1 molecule. Aminoacid electrophoresis indicated that phosphate was incorporated on serine residues. The phosphorylation effect of laminin-1 on the process of self assembly was studied by turbidometry. In these experiments, the phosphorylated laminin-1 showed a reduced maximal aggregation capacity in comparison to the non-phosphorylated molecule. Examination of the laminin-1 network under the electron microscope showed that the phosphorylated sample formed mainly linear extended oligomers, in contrast to controls that formed large and dense multimeric aggregates. Heparin binding on phosphorylated laminin-1 in comparison to controls was also tested using solid-phase binding assays. The results indicated an enhanced heparin binding to the phosphorylated protein. The results of this study indicate that laminin1-nidogen1 is a substrate for protein kinase A in vitro. This phosphorylation had an obvious influence on the lamininl-nidogen1 network formation and the heparin binding capacity of this molecule. However, further studies are needed to investigate whether or not this phenomenon could play a role in the formation of the structure of basement membranes in vivo.
Monocyte Attachment and Migration through Collagen IV in Diabetes Mellitus
Elena Kostidou,George Koliakos,Konstantinos Paletas,Martha Kaloyianni 한국분자세포생물학회 2008 Molecules and cells Vol.25 No.3
The interactions between monocytes and extracellular matrix proteins have been implicated in atherosclerosis pathophysiology. In the present study we evaluated monocyte attachment and migration through oxidized and non-oxidized collagen IV. Monocyte attachment was tested on microwells coated with either native or oxidized collagen IV. Monocyte migration through collagen IV was examined on transwells. Monocytes derived from patients with diabetes mellitus showed an increased ability to attach and migrate through collagen IV as compared to those derived from healthy volunteers. Moreover, control monocytes attached to oxidized collagen at a higher degree, while they migrated through oxidized collagen at a lower degree, as compared to the native protein. Our results also showed the involvement of the alpha2 integrin subunit in the above phenomena suggesting a modified interaction between monocytes and collagen IV in diabetes mellitus.
Iro Koliakou,Eleni Gounari,Maria Nerantzaki,Eleni Pavlidou,Dimitrios Bikiaris,Martha Kaloyianni,George Koliakos 한국조직공학과 재생의학회 2019 조직공학과 재생의학 Vol.16 No.2
BACKGROUND: Lonocyte-derived multipotential cells (MOMCs) include progenitors capable of differentiation into multiple cell lineages and thus represent an ideal autologous transplantable cell source for regenerative medicine. In this study, we cultured MOMCs, generated from mononuclear cells of peripheral blood, on the surface of nanocomposite thin films. METHODS: For this purpose, nanocomposite Poly(e-caprolactone) (PCL)-based thin films containing either 2.5 wt% silica nanotubes (SiO2ntbs) or strontium hydroxyapatite nanorods (SrHAnrds), were prepared using the spin-coating method. The induced differentiation capacity of MOMCs, towards bone and endothelium, was estimated using flow cytometry, real-time polymerase chain reaction, scanning electron microscopy and fluorescence microscopy after cells’ genetic modification using the Sleeping Beauty Transposon System aiming their observation onto the scaffolds. Moreover, Wharton’s Jelly Mesenchymal Stromal Cells were cultivated as a control cell line, while Human Umbilical Vein Endothelial Cells were used to strengthen and accelerate the differentiation procedure in semi-permeable culture systems. Finally, the cytotoxicity of the studied materials was checked with MTT assay. RESULTS: The highest differentiation capacity of MOMCs was observed on PCL/SiO2ntbs 2.5 wt% nanocomposite film, as they progressively lost their native markers and gained endothelial lineage, in both protein and transcriptional level. In addition, the presence of SrHAnrds in the PCL matrix triggered processes related to osteoblast bone formation. CONCLUSION: To conclude, the differentiation of MOMCs was selectively guided by incorporating SiO2ntbs or SrHAnrds into a polymeric matrix, for the first time.